Abstract
Wild and cultivated maize, sorghum, rice, amaranth, soybean, and cassava were screened for variability in seed storage proteins. Total seed proteins, albumin (Alb-1 and Alb-2), globulin, alcohol-soluble (A1 and A2), and glutelin (G1 and G2)fractions were investigated by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The comparison was done by the obtained protein patterns and their relative amounts. Using quantitative analysis of the protein composition and the electrophoretic patterns, the relationships between total proteins and amount of individual proteins were determined. Electrophoretic patterns of extracted proteins from investigated samples showed that the main protein subunits were concentrated between 10 and 45 kDa. Variation was found in major fractions and minor bands. Electrophoretic patterns of the protein fractions are directly related to the genetic background of the protein and can be identified and used to certify the genetic makeup of wild, cultivated, or newly derived cereals and plants.
| Original language | English |
|---|---|
| Pages (from-to) | 687-693 |
| Number of pages | 7 |
| Journal | Journal of Protein Chemistry |
| Volume | 18 |
| Issue number | 6 |
| DOIs | |
| State | Published - 1999 |
Keywords
- Composition
- Electrophoresis
- Plants
- Proteins
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